6RLA

Structure of the dynein-2 complex; motor domains

6RLA の概要

• エントリーDOI: 10.2210/pdb6rla/pdb
• EMDBエントリー: 4917
• 分子名称: O6-alkylguanine-DNA alkyltransferase mutant,DYNC2H1 variant protein, ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: dynein, cilia, intraflagellar transport, complex, motor protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 1034072.24

構造登録者

Toropova, K.,Zalyte, R.,Mukhopadhyay, A.G.,Mladenov, M.,Carter, A.P.,Roberts, A.J. (登録日: 2019-05-01, 公開日: 2019-08-28, 最終更新日: 2024-05-22)

主引用文献

Toropova, K.,Zalyte, R.,Mukhopadhyay, A.G.,Mladenov, M.,Carter, A.P.,Roberts, A.J.
Structure of the dynein-2 complex and its assembly with intraflagellar transport trains.
Nat.Struct.Mol.Biol., 26:823-829, 2019

PubMed Abstract: Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM structure to near-atomic resolution. The two identical copies of the dynein-2 heavy chain are contorted into different conformations by a WDR60-WDR34 heterodimer and a block of two RB and six LC8 light chains. One heavy chain is steered into a zig-zag conformation, which matches the periodicity of the anterograde IFT-B train. Contacts between adjacent dyneins along the train indicate a cooperative mode of assembly. Removal of the WDR60-WDR34-light chain subcomplex renders dynein-2 monomeric and relieves autoinhibition of its motility. Our results converge on a model in which an unusual stoichiometry of non-motor subunits controls dynein-2 assembly, asymmetry, and activity, giving mechanistic insight into the interaction of dynein-2 with IFT trains and the origin of diverse functions in the dynein family.

PubMed: 31451806
DOI: 10.1038/s41594-019-0286-y

実験手法

ELECTRON MICROSCOPY (3.9 Å)